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Inactivation of Animal and Human Prions by Hydrogen Peroxide Gas Plasma Sterilization

Published online by Cambridge University Press:  02 January 2015

C. Rogez-Kreuz ,
R. Yousfi ,
C. Soufflet ,
I. Quadrio ,
Z.-X. Yan ,
V. Huyot ,
C. Aubenque ,
P. Destrez ,
K. Roth  and
C. Roberts
...Show all authors
C. Rogez-Kreuz
Affiliation:
Neurovirology Laboratory, SPI-BIO, CEA, Fontenay aux Roses, France
R. Yousfi
Affiliation:
Neurovirology Laboratory, SPI-BIO, CEA, Fontenay aux Roses, France
C. Soufflet
Affiliation:
Advanced Sterilization Products, Division of Ethicon, Johnson & Johnson, Irvine, California
I. Quadrio
Affiliation:
Neurobiology Department, Centre de Biologie et Pathologie Est, Hospices Civils de Lyon, Bron, France
Z.-X. Yan
Affiliation:
Service fur Medizinprodukte, Tübingen, Germany
V. Huyot
Affiliation:
Neurovirology Laboratory, SPI-BIO, CEA, Fontenay aux Roses, France
C. Aubenque
Affiliation:
Neurovirology Laboratory, SPI-BIO, CEA, Fontenay aux Roses, France
P. Destrez
Affiliation:
Advanced Sterilization Products, Division of Ethicon, Johnson & Johnson, Irvine, California
K. Roth
Affiliation:
Service fur Medizinprodukte, Tübingen, Germany
C. Roberts*
Affiliation:
Advanced Sterilization Products, Division of Ethicon, Johnson & Johnson, Irvine, California
M. Favero
Affiliation:
Advanced Sterilization Products, Division of Ethicon, Johnson & Johnson, Irvine, California
P. Clayette
Affiliation:
Neurovirology Laboratory, SPI-BIO, CEA, Fontenay aux Roses, France
*
33 Technology Dr., Irvine, CA 92618 (crobert2@its.jnj.com)
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Abstract

Prions cause various transmissible spongiform encephalopathies. They are highly resistant to the chemical and physical decontamination and sterilization procedures routinely used in healthcare facilities. The decontamination procedures recommended for the inactivation of prions are often incompatible with the materials used in medical devices. In this study, we evaluated the use of low-temperature hydrogen peroxide gas plasma sterilization systems and other instrument-processing procedures for inactivating human and animal prions. We provide new data concerning the efficacy of hydrogen peroxide against prions from in vitro or in vivo tests, focusing on the following: the efficiency of hydrogen peroxide sterilization and possible interactions with enzymatic or alkaline detergents, differences in the efficiency of this treatment against different prion strains, and the influence of contaminating lipids. We found that gaseous hydrogen peroxide decreased the infectivity of prions and/or the level of the protease-resistant form of the prion protein on different surface materials. However, the efficiency of this treatment depended strongly on the concentration of hydrogen peroxide and the delivery system used in medical devices, because these effects were more pronounced for the new generation of Sterrad technology. The Sterrad NX sterilizer is 100% efficient (0% transmission and no protease-resistant form of the prion protein signal detected on the surface of the material for the mouse-adapted bovine spongiform encephalopathy 6PB1 strain and a variant Creutzfeldt-Jakob disease strain). Thus, gaseous or vaporized hydrogen peroxide efficiently inactivates prions on the surfaces of medical devices.

Type
Review Article
Information
Infection Control & Hospital Epidemiology , Volume 30 , Issue 8 , August 2009 , pp. 769 - 777
Copyright
Copyright © The Society for Healthcare Epidemiology of America 2009

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References

1.Legname, G, Baskakov, IV, Nguyen, HO, et al.Synthetic mammalian prions. Science 2004;305:673–676.CrossRefGoogle ScholarPubMed
2.Bolton, DC, McKinley, MP, Prusiner, SB. Identification of a protein that purifies with the scrapie prion. Science 1982;218:1309–1311.Google Scholar
3.Oesch, B, Westaway, D, Wälchli, M, et al.A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985;40:735–746.Google Scholar
4.Wadsworth, JDF, Collinge, J. Update on human prion disease. Biochim Biophys Acta 2007;1772:598–609.Google Scholar
5.Llewelyn, CA, Hewitt, PE, Knight, RS, et al.Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 2004;363:417–421.CrossRefGoogle ScholarPubMed
6.Peden, AH, Head, MW, Ritchie, DL, Bell, JE, Ironside, J. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 2004;364:527–529.CrossRefGoogle Scholar
7.Wroe, S, Pal, S, Siddique, D, et al.Clinical presentation and premortem diagnosis of blood transfusion associated variant Creutzfeldt-Jakob disease: a case report. Lancet 2006;368:2061–2067.Google Scholar
8.Collinge, J. Variant Creutzfeldt-Jakob disease. Lancet 1999;354:317–323.CrossRefGoogle ScholarPubMed
9.Joiner, S, Linehan, JM, Brander, S, Wadsworth, JDF, Collinge, J. High levels of disease-related prion protein in the ileum in variant Creutzfeldt-Jakob disease. Gut 2005;54:1506–1508.CrossRefGoogle ScholarPubMed
10.Wadsworth, JD, Joiner, S, Fox, K, et al.Prion infectivity in variant Creutzfeldt-Jakob disease rectum. Gut 2007;56:90–94.CrossRefGoogle ScholarPubMed
11.Wadsworth, JD, Joiner, S, Hill, AF, et al.Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet 2001;358:171–180.Google Scholar
12.Taylor, DM. Inactivation of transmissible degenerative encephalopathy agents: a review. Vet J 2000;159:10–17.CrossRefGoogle ScholarPubMed
13.French Ministry of Employment and Solidarity, and Ministry of Health. Guideline related to precautions to be observed during care to reduce the transmission of agents of nonconventional DGS/5C/DHOS/E2/2001/138. March 14, 2001. Available at http://www.sante-sports.gouv.fr/fi-chiers/bo/2001/01-ll/a0110756.htm. Accessed June 24, 2009.Google Scholar
14.Yang, S, Thackray, AM, Fitzmaurice, TJ, Bujdoso, R. Copper-induced structural changes in the ovine prion protein are influenced by a polymorphism at codon 112. Biochim Biophys Acta 2008;1784:683–692.Google Scholar
15.Fichet, G, Antloga, K, Comoy, E, Deslys, JP, McDonnell, G. Prion inactivation using a new gaseous hydrogen peroxide sterilisation process. J Hosp Infect 2007;67:278–286.CrossRefGoogle ScholarPubMed
16.Fichet, G, Comoy, E, Duval, C, et al.Novel methods for disinfection of prion-contaminated medical devices. Lancet 2004;364:521–526.CrossRefGoogle ScholarPubMed
17.Yan, ZX, Stitz, L, Heeg, P, Pfaff, E, Roth, K. Infectivity of prion protein bound to stainless steel wires: a model for testing decontamination procedures for transmissible spongiform encephalopathies. Infect Control Hosp Epidemiol 2004;25:280–283.CrossRefGoogle Scholar
18.Appel, TR, Wolff, M, von Rheinbaden, F, Heinzel, M, Reisner, D. Heat stability of prion rods and recombinant prion protein in water, lipid, and lipid-water mixtures. J Gen Virol 2001;82:465–473.Google Scholar
19.Adjou, KT, Demaimay, R, Lasmézas, C, Deslys, JP, Seman, M. MS-8209, a new amphotericin B derivative, provides enhanced efficacy in delaying hamster scrapie. Antimicrob Agents Chemother 1995;39:2810–2812.Google Scholar
20.Lasmézas, C, Deslys, JP, Demaimay, R, Adjou, KT, Hauw, JJ, Dormont, D. Strain specific and common pathogenic events in murine models of scrapie and bovine spongiform encephalopathy. J Gen Virol 1996;77:1601–1609.CrossRefGoogle ScholarPubMed
21.Bach, S, Talarek, N, Andrieu, T, et al.Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat Biotechnol 2003;21:1075–1081.Google Scholar
22.Müller, H, Stitz, L, Wille, H, Prusiner, SB, Reisner, D. Influence of water, fat, and glycerol on the mechanism of thermal prion inactivation. J Biol Chem 2007;282:35855–35867.Google Scholar
23.Lemmer, K, Mielke, M, Pauli, G, Beekes, M. Decontamination of surgical instruments from prion proteins: in vitro studies on the detachment, destabilization and degradation of PrPSc bound to steel surfaces. J Gen Virol 2004;85:3805–3816.CrossRefGoogle ScholarPubMed
24.Kärber, G. Beitrag zur kollektiven behandlung pharmakologischer reihenversuche [in German]. Arch Exp Pathol Pharmakol 1931;162:956–959.CrossRefGoogle Scholar
25.Lewin, P. Infectious peptides in slow virus infections: a hypothesis. Can Med Assoc J 1981;124:1436–1437.Google Scholar
26.Baxter, HC, Campbell, GA, Whittaker, AG, et al.Elimination of transmissible spongiform encephalopathy infectivity and decontamination of surgical instruments by using radio-frequency gas-plasma treatment. J Gen Virol 2005;86:2393–2399.Google Scholar
27.Jackson, GS, McKintosh, E, Flechsig, E, et al.An enzyme-detergent method for effective prion decontamination of surgical steel. J Gen Virol 2005;86:869–878.Google Scholar
28.Asher, DM, Pomeroy, KL, Murphy, L, Rohwer, RG, Gibbs, CJ, Gajdusek, DC. Attempts to disinfect surfaces contaminated with etiological agents of the spongiform encephalopathies. In: Program and abstracts of the 7th International Congress of Virology; 1987; Edmonton, Alberta, Canada.Google Scholar
29.Asher, DM, Pomeroy, KL, Murphy, L, Rohwer, RG, Gibbs, CJ, Gajdusek, DC. Practical inactivation of scrapie agent on surfaces. In: Program and abstracts of the 9th International Congress of Infectious and Parasitic Diseases; 1986; Munich, Germany.Google Scholar
30.Caughey, B, Ernst, D, Race, RE. Congo red inhibition of scrapie agent replication. J Virol 1993;67:6270–6272.Google Scholar
31.McDonnell, G, Burke, P. The challenge of prion decontamination. Clin Infect Dis 2003;36:1152–1154.CrossRefGoogle ScholarPubMed